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Publication Abstract from PubMed
The ultraviolet damage endonuclease (UVDE) performs the initial step in an alternative excision repair pathway of UV-induced DNA damage, nicking immediately adjacent to the 5' phosphate of the damaged nucleotides. Unique for a single-protein DNA repair endonuclease, it can detect different types of damage. Here we show that Thermus thermophilus UVDE shares some essential structural features with Endo IV, an enzyme from the base excision repair pathway that exclusively nicks at abasic sites. A comparison between the structures indicates how DNA is bound by UVDE, how UVDE may recognize damage, and which of its residues are involved in catalysis. Furthermore, the comparison suggests an elegant explanation of UVDE's potential to recognize different types of damage. Incision assays including point mutants of UVDE confirmed the relevance of these conclusions.
Crystal structure of the DNA repair enzyme ultraviolet damage endonuclease.,Paspaleva K, Thomassen E, Pannu NS, Iwai S, Moolenaar GF, Goosen N, Abrahams JP Structure. 2007 Oct;15(10):1316-24. PMID:17937920[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑Paspaleva K, Thomassen E, Pannu NS, Iwai S, Moolenaar GF, Goosen N, Abrahams JP. Crystal structure of the DNA repair enzyme ultraviolet damage endonuclease. Structure. 2007 Oct;15(10):1316-24. PMID:17937920 doi:10.1016/j.str.2007.05.010
